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Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Publication date 2013
Author Santi Sara, Musi Valeria, Descrovi Emiliano, Paeder Vincent, Di Francesco Joab, Hvozdara Lubos, van der Wal Peter, Lashuel Hilal A., Pastore Annalisa, Neier Reinhard, Herzig Hans Peter,
Project The hydrogenation of calix[4]pyrroles leading to the novel ligand system calix[4]pyrrolidine: Their properties and their application
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Original article (peer-reviewed)

Journal CHEMPHYSCHEM
Volume (Issue) 14(15)
Page(s) 3476 - 3482
Title of proceedings CHEMPHYSCHEM
DOI 10.1002/cphc.201300633

Abstract

We propose the application of a new label-free optical technique based on photonic nanostructures to real-time monitor the amyloidbeta 1-42 (Aβ(1-42)) fibrillization, including the early stages of the aggregation process, which are related to the onset of the Alzheimer’s Disease (AD). The aggregation of Aβ peptides into amyloid fibrils has commonly been associated with neuronal death, which culminates in the clinical features of the incurable degenerative AD. Recent studies revealed that cell toxicity is determined by the formation of soluble oligomeric forms of Aβ peptides in the early stages of aggregation. At this phase, classical amyloid detection techniques lack in sensitivity. Upon a chemical passivation of the sensor surface by means of polyethylene glycol, the proposed approach allows an accurate, realtime monitoring of the refractive index variation of the solution, wherein Aβ(1-42) peptides are aggregating. This measurement is directly related to the aggregation state of the peptide throughout oligomerization and subsequent fibrillization. Our findings open new perspectives in the understanding of the dynamics of amyloid formation, and validate this approach as a new and powerful method to screen aggregation at early stages.
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